Rat p67 GBP is induced by interferon-gamma and isoprenoid-modified in macrophages
| Autor: | Vinod Asundi, Gregory S. Kelner, Dominique Maciejewski, Janice E. Buss, Richard A. Maki, Deborah J. Vestal |
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| Rok vydání: | 1996 |
| Předmět: |
Lipopolysaccharides
Immunoblotting Molecular Sequence Data Biophysics Protein Prenylation Mevalonic Acid Bone Marrow Cells Biology Biochemistry Polymerase Chain Reaction Rats Sprague-Dawley Interferon-gamma GTP-binding protein regulators Prenylation Interferon GTP-Binding Proteins medicine Animals Interferon gamma Molecular Biology Cells Cultured DNA Primers COS cells Microglia Base Sequence Macrophages Cell Biology Transfection Molecular biology Rats Molecular Weight medicine.anatomical_structure Animals Newborn Protein prenylation medicine.drug |
| Zdroj: | Biochemical and biophysical research communications. 224(2) |
| ISSN: | 0006-291X |
| Popis: | The guanylate binding proteins, GBPs, are a family of interferon-induced GTP-binding proteins that include the rat p67. We report here that rat p67, for which interferon regulation had not previously been demonstrated, is induced by IFN-gamma and also by LPS in both cultured bone marrow-derived macrophages and microglia. The basal level of rat p67 in macrophages is low but increases dramatically between 2 and 4 hours after treating cells with either IFN-gamma or LPS. It then remains elevated over the next 24 hours. Rat p67 is isoprenoid modified. The isoprenoid modification was detected in p67 isolated both from primary IFN-gamma-activated macrophages and when the gene for p67 was transfected into COS cells. This is the first demonstration of in vivo prenylation of a GBP. The interferon regulation and prenylation of rat p67 point toward this protein being significant in the functions of both activated macrophages and microglia. |
| Databáze: | OpenAIRE |
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